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Database: UniProt
Entry: A0A172XQY7_9FLAO
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ID   A0A172XQY7_9FLAO        Unreviewed;       272 AA.
AC   A0A172XQY7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Undecaprenyl-diphosphatase {ECO:0000256|ARBA:ARBA00021581, ECO:0000256|HAMAP-Rule:MF_01006};
DE            EC=3.6.1.27 {ECO:0000256|ARBA:ARBA00012374, ECO:0000256|HAMAP-Rule:MF_01006};
DE   AltName: Full=Bacitracin resistance protein {ECO:0000256|ARBA:ARBA00032932, ECO:0000256|HAMAP-Rule:MF_01006};
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00032707, ECO:0000256|HAMAP-Rule:MF_01006};
GN   Name=uppP {ECO:0000256|HAMAP-Rule:MF_01006};
GN   ORFNames=A0O34_02145 {ECO:0000313|EMBL:ANF49429.1};
OS   Chryseobacterium glaciei.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1685010 {ECO:0000313|EMBL:ANF49429.1, ECO:0000313|Proteomes:UP000077824};
RN   [1] {ECO:0000313|EMBL:ANF49429.1, ECO:0000313|Proteomes:UP000077824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHBB 10212 {ECO:0000313|EMBL:ANF49429.1,
RC   ECO:0000313|Proteomes:UP000077824};
RA   Pal M., Swarnkar M.K., Kaushal K., Chhibber S., Singh A.K., Gulati A.;
RT   "Complete Genome Sequence of Chryseobacterium sp. IHBB 10212.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC       (UPP). Confers resistance to bacitracin. {ECO:0000256|HAMAP-
CC       Rule:MF_01006}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-
CC         trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:28094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58405, ChEBI:CHEBI:60392; EC=3.6.1.27;
CC         Evidence={ECO:0000256|ARBA:ARBA00000759, ECO:0000256|HAMAP-
CC         Rule:MF_01006};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01006};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01006}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- MISCELLANEOUS: Bacitracin is thought to be involved in the inhibition
CC       of peptidoglycan synthesis by sequestering undecaprenyl diphosphate,
CC       thereby reducing the pool of lipid carrier available.
CC       {ECO:0000256|HAMAP-Rule:MF_01006}.
CC   -!- SIMILARITY: Belongs to the UppP family. {ECO:0000256|ARBA:ARBA00010621,
CC       ECO:0000256|HAMAP-Rule:MF_01006}.
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DR   EMBL; CP015199; ANF49429.1; -; Genomic_DNA.
DR   RefSeq; WP_066750812.1; NZ_CP015199.1.
DR   AlphaFoldDB; A0A172XQY7; -.
DR   STRING; 1685010.A0O34_02145; -.
DR   KEGG; chh:A0O34_02145; -.
DR   OrthoDB; 9808289at2; -.
DR   Proteomes; UP000077824; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01006; Undec_diphosphatase; 1.
DR   InterPro; IPR003824; UppP.
DR   PANTHER; PTHR30622; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR   PANTHER; PTHR30622:SF3; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR   Pfam; PF02673; BacA; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251, ECO:0000256|HAMAP-
KW   Rule:MF_01006};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01006}; Cell shape {ECO:0000256|HAMAP-Rule:MF_01006};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01006};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01006};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01006};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01006};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01006};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01006}.
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        73..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        97..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        179..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        220..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        254..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   272 AA;  30331 MW;  CB739D7FDB2D8E1F CRC64;
     MDLIKAIVIA IIEGLTEYLP ISSTAHMGFA ANLMGMQEDE FLKMFQVSIQ FGAILSVVVA
     YWKKFFDFNN IKFYFKLAYA VVPALVLGYL FDDKIEAILG NQIAISSVLV LGGVVLLFAD
     KWFKNPTIDD EKGITVKKAI TIGFWQCLAM MPGTSRSAAS IIGGMTQGLT RKAAAEFSFF
     LAVPTMLAVT VYSVFVKTWG KETPNPQKGY EMIMSSNDHI MIFVIGNVVA FIVALIAIKA
     FIGVLNKYGF KPWGWYRIFV GLALLIYFYF FK
//
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